PRIO_MESAU
ID PRIO_MESAU Reviewed; 254 AA.
AC P04273;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Major prion protein;
DE Short=PrP;
DE AltName: Full=PrP27-30;
DE AltName: Full=PrP33-35C;
DE AltName: CD_antigen=CD230;
DE Flags: Precursor;
GN Name=PRNP; Synonyms=PRP;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2873895; DOI=10.1016/0092-8674(86)90662-8;
RA Basler K., Oesch B., Scott M., Westaway D., Waelchli M., Groth D.F.,
RA McKinley M.P., Prusiner S.B., Weissmann C.;
RT "Scrapie and cellular PrP isoforms are encoded by the same chromosomal
RT gene.";
RL Cell 46:417-428(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-254.
RX PubMed=2859120; DOI=10.1016/0092-8674(85)90333-2;
RA Oesch B., Westaway D., Walchli M., McKinley M.P., Kent S.B.H.,
RA Aebersold R., Barry R.A., Tempst P., Teplow D.B., Hood L.E., Prusiner S.B.,
RA Weissmann C.;
RT "A cellular gene encodes scrapie PrP 27-30 protein.";
RL Cell 40:735-746(1985).
RN [3]
RP GLYCOSYLATION AT ASN-181 AND ASN-197, AND DISULFIDE BONDS.
RX PubMed=3138115; DOI=10.1111/j.1432-1033.1988.tb14246.x;
RA Turk E., Teplow D.B., Hood L.E., Prusiner S.B.;
RT "Purification and properties of the cellular and scrapie hamster prion
RT proteins.";
RL Eur. J. Biochem. 176:21-30(1988).
RN [4]
RP GPI-ANCHOR.
RX PubMed=2444340; DOI=10.1016/0092-8674(87)90150-4;
RA Stahl N., Borchelt D.R., Hasiao K., Prusiner S.B.;
RT "Scrapie prion protein contains a phosphatidylinositol glycolipid.";
RL Cell 51:229-240(1987).
RN [5]
RP GPI-ANCHOR AT SER-231.
RX PubMed=1980209; DOI=10.1021/bi00490a001;
RA Stahl N., Baldwin M.A., Burlingame A.L., Prusiner S.B.;
RT "Identification of glycoinositol phospholipid linked and truncated forms of
RT the scrapie prion protein.";
RL Biochemistry 29:8879-8884(1990).
RN [6]
RP MUTAGENESIS OF THR-183 AND THR-199.
RX PubMed=1983782; DOI=10.1093/glycob/1.1.101;
RA Rogers M., Taraboulos A., Scott M., Groth D., Prusiner S.B.;
RT "Intracellular accumulation of the cellular prion protein after mutagenesis
RT of its Asn-linked glycosylation sites.";
RL Glycobiology 1:101-109(1990).
RN [7]
RP COPPER- OR ZINC-BINDING SITES, AND DOMAIN.
RX PubMed=12779334; DOI=10.1021/bi027138+;
RA Burns C.S., Aronoff-Spencer E., Legname G., Prusiner S.B., Antholine W.E.,
RA Gerfen G.J., Peisach J., Millhauser G.L.;
RT "Copper coordination in the full-length, recombinant prion protein.";
RL Biochemistry 42:6794-6803(2003).
RN [8]
RP COPPER-BINDING.
RX PubMed=16144413; DOI=10.1021/ja053254z;
RA Chattopadhyay M., Walter E.D., Newell D.J., Jackson P.J.,
RA Aronoff-Spencer E., Peisach J., Gerfen G.J., Bennett B., Antholine W.E.,
RA Millhauser G.L.;
RT "The octarepeat domain of the prion protein binds Cu(II) with three
RT distinct coordination modes at pH 7.4.";
RL J. Am. Chem. Soc. 127:12647-12656(2005).
RN [9]
RP COPPER-BINDING, AND ZINC-BINDING.
RX PubMed=18034490; DOI=10.1021/ja077146j;
RA Walter E.D., Stevens D.J., Visconte M.P., Millhauser G.L.;
RT "The prion protein is a combined zinc and copper binding protein: Zn2+
RT alters the distribution of Cu2+ coordination modes.";
RL J. Am. Chem. Soc. 129:15440-15441(2007).
RN [10]
RP RETRACTED PAPER.
RX PubMed=19059915; DOI=10.1074/jbc.m804051200;
RA Juanes M.E., Elvira G., Garcia-Grande A., Calero M., Gasset M.;
RT "Biosynthesis of prion protein nucleocytoplasmic isoforms by alternative
RT initiation of translation.";
RL J. Biol. Chem. 284:2787-2794(2009).
RN [11]
RP RETRACTION NOTICE OF PUBMED:19059915.
RX PubMed=29222195; DOI=10.1074/jbc.w117.000658;
RA Juanes M.E., Elvira G., Garcia-Grande A., Calero M., Gasset M.;
RT "Biosynthesis of prion protein nucleocytoplasmic isoforms by alternative
RT initiation of translation.";
RL J. Biol. Chem. 292:20044-20044(2017).
RN [12]
RP COPPER-BINDING.
RX PubMed=19381258; DOI=10.1371/journal.ppat.1000390;
RA Stevens D.J., Walter E.D., Rodriguez A., Draper D., Davies P., Brown D.R.,
RA Millhauser G.L.;
RT "Early onset prion disease from octarepeat expansion correlates with copper
RT or zinc binding properties.";
RL PLoS Pathog. 5:E1000390-E1000390(2009).
RN [13]
RP STRUCTURE BY NMR OF 90-231.
RX PubMed=9294167; DOI=10.1073/pnas.94.19.10086;
RA James T.L., Liu H., Ulyanov N.B., Farr-Jones S., Zhang H., Donne D.G.,
RA Kaneko K., Groth D., Mehlhorn I., Prusiner S.B., Cohen F.E.;
RT "Solution structure of a 142-residue recombinant prion protein
RT corresponding to the infectious fragment of the scrapie isoform.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:10086-10091(1997).
RN [14]
RP STRUCTURE BY NMR OF 29-231.
RX PubMed=9391046; DOI=10.1073/pnas.94.25.13452;
RA Donne D.G., Viles J.H., Groth D., Mehlhorn I., James T.L., Cohen F.E.,
RA Prusiner S.B., Wright P.E., Dyson H.J.;
RT "Structure of the recombinant full-length hamster prion protein PrP(29-
RT 231): the N-terminus is highly flexible.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13452-13457(1997).
CC -!- FUNCTION: Its primary physiological function is unclear. May play a
CC role in neuronal development and synaptic plasticity. May be required
CC for neuronal myelin sheath maintenance. May promote myelin homeostasis
CC through acting as an agonist for ADGRG6 receptor. May play a role in
CC iron uptake and iron homeostasis. Soluble oligomers are toxic to
CC cultured neuroblastoma cells and induce apoptosis (in vitro) (By
CC similarity). Association with GPC1 (via its heparan sulfate chains)
CC targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the
CC ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate
CC side chains (By similarity). {ECO:0000250|UniProtKB:P04156,
CC ECO:0000250|UniProtKB:P04925}.
CC -!- SUBUNIT: Monomer and homodimer. Has a tendency to aggregate into
CC amyloid fibrils containing a cross-beta spine, formed by a steric
CC zipper of superposed beta-strands. Soluble oligomers may represent an
CC intermediate stage on the path to fibril formation. Copper binding may
CC promote oligomerization. Interacts with GRB2, APP, ERI3/PRNPIP and SYN1
CC (By similarity). Mislocalized cytosolically exposed PrP interacts with
CC MGRN1; this interaction alters MGRN1 subcellular location and causes
CC lysosomal enlargement (By similarity). Interacts with APP. Interacts
CC with KIAA1191 (By similarity). Interacts with ADGRG6 (By similarity).
CC {ECO:0000250|UniProtKB:P04156, ECO:0000250|UniProtKB:P04925}.
CC -!- INTERACTION:
CC P04273; P04273: PRNP; NbExp=10; IntAct=EBI-986426, EBI-986426;
CC P04273; Q8CJG0: Ago2; Xeno; NbExp=2; IntAct=EBI-986426, EBI-528299;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04156};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P04156}. Golgi
CC apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts
CC via association with the heparan sulfate chains of GPC1. Colocates, in
CC the presence of Cu(2+), to vesicles in para- and perinuclear regions,
CC where both proteins undergo internalization. Heparin displaces PRNP
CC from lipid rafts and promotes endocytosis.
CC {ECO:0000250|UniProtKB:P04156}.
CC -!- DOMAIN: The normal, monomeric form has a mainly alpha-helical
CC structure. The disease-associated, protease-resistant form forms
CC amyloid fibrils containing a cross-beta spine, formed by a steric
CC zipper of superposed beta-strands. Disease mutations may favor
CC intermolecular contacts via short beta strands, and may thereby trigger
CC oligomerization. {ECO:0000250|UniProtKB:P04156}.
CC -!- DOMAIN: Contains an N-terminal region composed of octamer repeats. At
CC low copper concentrations, the sidechains of His residues from three or
CC four repeats contribute to the binding of a single copper ion.
CC Alternatively, a copper ion can be bound by interaction with the
CC sidechain and backbone amide nitrogen of a single His residue. The
CC observed copper binding stoichiometry suggests that two repeat regions
CC cooperate to stabilize the binding of a single copper ion. At higher
CC copper concentrations, each octamer can bind one copper ion by
CC interactions with the His sidechain and Gly backbone atoms. A mixture
CC of binding types may occur, especially in the case of octamer repeat
CC expansion. Copper binding may stabilize the conformation of this region
CC and may promote oligomerization. {ECO:0000250|UniProtKB:P04156}.
CC -!- DISEASE: Note=Found in high quantity in the brain of humans and animals
CC infected with degenerative neurological diseases such as kuru,
CC Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS),
CC scrapie, bovine spongiform encephalopathy (BSE), transmissible mink
CC encephalopathy (TME), etc. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the prion family. {ECO:0000305}.
CC -!- CAUTION: An isoform was shown to be localized to both the cytoplasm and
CC the nucleus and to be sumoylated with SUMO1 (PubMed:19059915). The
CC article has later been withdrawn by the authors.
CC {ECO:0000269|PubMed:19059915, ECO:0000305|PubMed:29222195}.
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DR EMBL; M14054; AAA37091.1; -; Genomic_DNA.
DR EMBL; K02234; AAA37092.1; -; mRNA.
DR PIR; I48168; UJHYIH.
DR RefSeq; XP_005068717.1; XM_005068660.2.
DR RefSeq; XP_012967855.1; XM_013112401.1.
DR PDB; 1B10; NMR; -; A=90-231.
DR PDB; 2KKG; NMR; -; A=23-106.
DR PDB; 2LH8; NMR; -; A=125-228.
DR PDB; 3NVE; X-ray; 1.70 A; A/B=138-143.
DR PDB; 4YXL; X-ray; 2.60 A; A=90-232.
DR PDB; 7LNA; EM; 3.10 A; A/B/C=90-231.
DR PDBsum; 1B10; -.
DR PDBsum; 2KKG; -.
DR PDBsum; 2LH8; -.
DR PDBsum; 3NVE; -.
DR PDBsum; 4YXL; -.
DR PDBsum; 7LNA; -.
DR AlphaFoldDB; P04273; -.
DR BMRB; P04273; -.
DR SMR; P04273; -.
DR DIP; DIP-1081N; -.
DR IntAct; P04273; 1.
DR STRING; 10036.XP_005068717.1; -.
DR BindingDB; P04273; -.
DR ChEMBL; CHEMBL1293203; -.
DR GlyConnect; 358; 8 N-Linked glycans.
DR iPTMnet; P04273; -.
DR MetOSite; P04273; -.
DR PRIDE; P04273; -.
DR ABCD; P04273; 10 sequenced antibodies.
DR GeneID; 101829062; -.
DR eggNOG; ENOG502S2A8; Eukaryota.
DR EvolutionaryTrace; P04273; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:1903135; F:cupric ion binding; IMP:CAFA.
DR GO; GO:1903136; F:cuprous ion binding; IEA:Ensembl.
DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0038023; F:signaling receptor activity; IEA:Ensembl.
DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
DR GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IEA:Ensembl.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0032700; P:negative regulation of interleukin-17 production; IEA:Ensembl.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1990535; P:neuron projection maintenance; IEA:Ensembl.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:1905664; P:regulation of calcium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:1900449; P:regulation of glutamate receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1902938; P:regulation of intracellular calcium activated chloride channel activity; IEA:Ensembl.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR DisProt; DP00187; -.
DR Gene3D; 1.10.790.10; -; 1.
DR InterPro; IPR000817; Prion.
DR InterPro; IPR036924; Prion/Doppel_b-ribbon_dom_sf.
DR InterPro; IPR022416; Prion/Doppel_prot_b-ribbon_dom.
DR InterPro; IPR025860; Prion_N_dom.
DR Pfam; PF00377; Prion; 1.
DR Pfam; PF11587; Prion_bPrPp; 1.
DR PRINTS; PR00341; PRION.
DR SMART; SM00157; PRP; 1.
DR SUPFAM; SSF54098; SSF54098; 1.
DR PROSITE; PS00291; PRION_1; 1.
DR PROSITE; PS00706; PRION_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amyloid; Cell cycle; Cell membrane; Copper; Disulfide bond;
KW Glycoprotein; Golgi apparatus; GPI-anchor; Growth arrest; Lipoprotein;
KW Membrane; Metal-binding; Prion; Reference proteome; Repeat; Signal; Zinc.
FT SIGNAL 1..22
FT CHAIN 23..231
FT /note="Major prion protein"
FT /id="PRO_0000025695"
FT PROPEP 232..254
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:1980209"
FT /id="PRO_0000025696"
FT REPEAT 51..59
FT /note="1"
FT REPEAT 60..67
FT /note="2"
FT REPEAT 68..75
FT /note="3"
FT REPEAT 76..83
FT /note="4"
FT REPEAT 84..91
FT /note="5"
FT REGION 23..231
FT /note="Interaction with GRB2, ERI3 and SYN1"
FT /evidence="ECO:0000250|UniProtKB:P04925"
FT REGION 23..38
FT /note="Interaction with ADGRG6"
FT /evidence="ECO:0000250|UniProtKB:P04925"
FT REGION 25..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..91
FT /note="5 X 8 AA tandem repeats of P-H-G-G-G-W-G-Q"
FT REGION 90..231
FT /note="PrP27-30 (protease resistant core)"
FT BINDING 61
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 62
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 63
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 69
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 70
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 71
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 77
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 78
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 79
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 85
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 86
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT BINDING 87
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P04156"
FT LIPID 231
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000269|PubMed:1980209"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3138115"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3138115"
FT DISULFID 179..214
FT /evidence="ECO:0000269|PubMed:3138115"
FT MUTAGEN 183
FT /note="T->A: Accumulates intracellularly."
FT /evidence="ECO:0000269|PubMed:1983782"
FT MUTAGEN 199
FT /note="T->A: Accumulates intracellularly."
FT /evidence="ECO:0000269|PubMed:1983782"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2KKG"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2KKG"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2KKG"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2KKG"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2KKG"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2KKG"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:7LNA"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:7LNA"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:7LNA"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:7LNA"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1B10"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3NVE"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:4YXL"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4YXL"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:7LNA"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4YXL"
FT HELIX 172..193
FT /evidence="ECO:0007829|PDB:4YXL"
FT HELIX 200..222
FT /evidence="ECO:0007829|PDB:4YXL"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:7LNA"
SQ SEQUENCE 254 AA; 27919 MW; 442C0E3ED4D20672 CRC64;
MANLSYWLLA LFVAMWTDVG LCKKRPKPGG WNTGGSRYPG QGSPGGNRYP PQGGGTWGQP
HGGGWGQPHG GGWGQPHGGG WGQPHGGGWG QGGGTHNQWN KPSKPKTNMK HMAGAAAAGA
VVGGLGGYML GSAMSRPMMH FGNDWEDRYY RENMNRYPNQ VYYRPVDQYN NQNNFVHDCV
NITIKQHTVT TTTKGENFTE TDIKIMERVV EQMCTTQYQK ESQAYYDGRR SSAVLFSSPP
VILLISFLIF LMVG
